Author:
Brown J.,Walter T. S.,Carter L.,Abrescia N. G. A.,Aricescu A. R.,Batuwangala T. D.,Bird L. E.,Brown N.,Chamberlain P. P.,Davis S. J.,Dubinina E.,Endicott J.,Fennelly J. A.,Gilbert R. J. C.,Harkiolaki M.,Hon W.-C.,Kimberley F.,Love C. A.,Mancini E. J.,Manso-Sancho R.,Nichols C. E.,Robinson R. A.,Sutton G. C.,Schueller N.,Sleeman M. C.,Stewart-Jones G. B.,Vuong M.,Welburn J.,Zhang Z.,Stammers D. K.,Owens R. J.,Jones E. Y.,Harlos K.,Stuart D. I.
Abstract
An initial tranche of results from day-to-day use of a robotic system for setting up 100 nl-scale vapour-diffusion sitting-drop protein crystallizations has been surveyed. The database of over 50 unrelated samples represents a snapshot of projects currently at the stage of crystallization trials in Oxford research groups and as such encompasses a broad range of proteins. The results indicate that the nanolitre-scale methodology consistently identifies more crystallization conditions than traditional hand-pipetting-style methods; however, in a number of cases successful scale-up is then problematic. Crystals grown in the initial 100 nl-scale drops have in the majority of cases allowed useful characterization of X-ray diffraction, either in-house or at synchrotron beamlines. For a significant number of projects, full X-ray diffraction data sets have been collected to 3 Å resolution or better (either in-house or at the synchrotron) from crystals grown at the 100 nl scale. To date, five structures have been determined by molecular replacement directly from such data and a further three from scale-up of conditions established at the nanolitre scale.
Publisher
International Union of Crystallography (IUCr)
Subject
General Biochemistry, Genetics and Molecular Biology
Cited by
43 articles.
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